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B8D903 (GUAC_BUCA5) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 34. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
GMP reductase

EC=1.7.1.7
Alternative name(s):
Guanosine 5'-monophosphate oxidoreductase
Short name=Guanosine monophosphate reductase
Gene names
Name:guaC
Ordered Locus Names:BUAP5A_201
OrganismBuchnera aphidicola subsp. Acyrthosiphon pisum (strain 5A) [Complete proteome] [HAMAP]
Taxonomic identifier563178 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length349 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides By similarity. HAMAP-Rule MF_00596

Catalytic activity

Inosine 5'-phosphate + NH3 + NADP+ = guanosine 5'-phosphate + NADPH. HAMAP-Rule MF_00596

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_00596

Sequence similarities

Belongs to the IMPDH/GMPR family. GuaC type 1 subfamily.

Ontologies

Keywords
   LigandMetal-binding
NADP
Potassium
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processpurine nucleotide metabolic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentGMP reductase complex

Inferred from electronic annotation. Source: UniProtKB-EC

   Molecular_functionGMP reductase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 349349GMP reductase HAMAP-Rule MF_00596
PRO_1000146983

Regions

Nucleotide binding108 – 13124NADP By similarity
Nucleotide binding216 – 23924NADP; ribose moiety By similarity

Sites

Active site1861Thioimidate intermediate By similarity
Metal binding1811Potassium; via carbonyl oxygen By similarity
Metal binding1831Potassium; via carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
B8D903 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: D4D109BD6B493D72

FASTA34938,320
        10         20         30         40         50         60 
MRIEEDIKLG FKDVLIRPKR SILKSRSQVN LARCFSFKYS ASIWSGIPII AANMDTIGTF 

        70         80         90        100        110        120 
EMVKSLSKFN ILTAVHKYYS FEEWKNFVCL SSKEILNHVI VSIGTSNIDF LKIKKIFLLS 

       130        140        150        160        170        180 
SELKYICIDV ANGYSEHIVS FLKLVRDYFP DKIICAGNVV TGEMVEELIL SGADIVKVGI 

       190        200        210        220        230        240 
GPGSVCTTRV KTGVGYPQLS AIIECADAAH GLNGQIISDG GCTVSGDIAK AFGGGADFVM 

       250        260        270        280        290        300 
LGGMLSGHKE CSGDIIEEKS KKYMIFYGMS SVSAMQRYEG KIAGYRASEG KTVKIPFRGG 

       310        320        330        340 
VDSTIRDILG GLRSSCTYVG AEKLKELTKR TTFIRVTEQE NCIFNAFKE 

« Hide

References

[1]"The dynamics and time scale of ongoing genomic erosion in symbiotic bacteria."
Moran N.A., McLaughlin H.J., Sorek R.
Science 323:379-382(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 5A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001161 Genomic DNA. Translation: ACL30574.1.
RefSeqYP_002467962.1. NC_011833.1.

3D structure databases

ProteinModelPortalB8D903.
SMRB8D903. Positions 3-338.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING107806.BU204.

Proteomic databases

PRIDEB8D903.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACL30574; ACL30574; BUAP5A_201.
GeneID7262711.
KEGGbap:BUAP5A_201.
PATRIC21242641. VBIBucAph51993_0202.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0516.
HOGENOMHOG000165756.
KOK00364.
OMACSCAGDV.
OrthoDBEOG6GTZPV.
ProtClustDBPRK05096.

Enzyme and pathway databases

BioCycBAPH563178:GHDF-201-MONOMER.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_00596. GMP_reduct_type1.
InterProIPR013785. Aldolase_TIM.
IPR005993. GMP_reduct1.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view]
PfamPF00478. IMPDH. 1 hit.
[Graphical view]
PIRSFPIRSF000235. GMP_reductase. 1 hit.
TIGRFAMsTIGR01305. GMP_reduct_1. 1 hit.
PROSITEPS00487. IMP_DH_GMP_RED. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGUAC_BUCA5
AccessionPrimary (citable) accession number: B8D903
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: February 19, 2014
This is version 34 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families